PMC:7253482 / 4198-5509 JSONTXT

{"project":"LitCovid-PubTator","denotations":[{"id":"171","span":{"begin":108,"end":111},"obj":"Species"},{"id":"172","span":{"begin":460,"end":468},"obj":"Species"},{"id":"173","span":{"begin":749,"end":754},"obj":"Species"},{"id":"174","span":{"begin":177,"end":189},"obj":"Chemical"},{"id":"175","span":{"begin":195,"end":202},"obj":"Chemical"},{"id":"176","span":{"begin":277,"end":284},"obj":"Chemical"},{"id":"177","span":{"begin":336,"end":343},"obj":"Chemical"},{"id":"178","span":{"begin":388,"end":400},"obj":"Chemical"},{"id":"179","span":{"begin":406,"end":413},"obj":"Chemical"},{"id":"180","span":{"begin":442,"end":448},"obj":"Chemical"},{"id":"181","span":{"begin":649,"end":665},"obj":"Chemical"},{"id":"182","span":{"begin":724,"end":730},"obj":"Chemical"},{"id":"183","span":{"begin":868,"end":874},"obj":"Chemical"},{"id":"184","span":{"begin":998,"end":1004},"obj":"Chemical"},{"id":"185","span":{"begin":1106,"end":1118},"obj":"Chemical"},{"id":"186","span":{"begin":1124,"end":1130},"obj":"Chemical"},{"id":"187","span":{"begin":1181,"end":1187},"obj":"Chemical"},{"id":"188","span":{"begin":88,"end":92},"obj":"Disease"},{"id":"189","span":{"begin":94,"end":98},"obj":"Disease"},{"id":"190","span":{"begin":504,"end":508},"obj":"Disease"},{"id":"191","span":{"begin":513,"end":517},"obj":"Disease"},{"id":"192","span":{"begin":740,"end":744},"obj":"Disease"},{"id":"193","span":{"begin":895,"end":899},"obj":"Disease"}],"attributes":[{"id":"A171","pred":"tao:has_database_id","subj":"171","obj":"Tax:11118"},{"id":"A172","pred":"tao:has_database_id","subj":"172","obj":"Tax:1335626"},{"id":"A173","pred":"tao:has_database_id","subj":"173","obj":"Tax:11676"},{"id":"A175","pred":"tao:has_database_id","subj":"175","obj":"MESH:D011134"},{"id":"A176","pred":"tao:has_database_id","subj":"176","obj":"MESH:D011134"},{"id":"A177","pred":"tao:has_database_id","subj":"177","obj":"MESH:D011134"},{"id":"A179","pred":"tao:has_database_id","subj":"179","obj":"MESH:D011134"},{"id":"A180","pred":"tao:has_database_id","subj":"180","obj":"MESH:D011134"},{"id":"A182","pred":"tao:has_database_id","subj":"182","obj":"MESH:D011134"},{"id":"A183","pred":"tao:has_database_id","subj":"183","obj":"MESH:D011134"},{"id":"A184","pred":"tao:has_database_id","subj":"184","obj":"MESH:D011134"},{"id":"A186","pred":"tao:has_database_id","subj":"186","obj":"MESH:D011134"},{"id":"A187","pred":"tao:has_database_id","subj":"187","obj":"MESH:D011134"},{"id":"A188","pred":"tao:has_database_id","subj":"188","obj":"MESH:D045169"},{"id":"A189","pred":"tao:has_database_id","subj":"189","obj":"MESH:D018352"},{"id":"A190","pred":"tao:has_database_id","subj":"190","obj":"MESH:D045169"},{"id":"A191","pred":"tao:has_database_id","subj":"191","obj":"MESH:D018352"},{"id":"A192","pred":"tao:has_database_id","subj":"192","obj":"MESH:D045169"},{"id":"A193","pred":"tao:has_database_id","subj":"193","obj":"MESH:D045169"}],"namespaces":[{"prefix":"Tax","uri":"https://www.ncbi.nlm.nih.gov/taxonomy/"},{"prefix":"MESH","uri":"https://id.nlm.nih.gov/mesh/"},{"prefix":"Gene","uri":"https://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"CVCL","uri":"https://web.expasy.org/cellosaurus/CVCL_"}],"text":"Here, we provide global and site-specific analyses of N-linked glycosylation on soluble SARS, MERS and HKU1 CoV S glycoproteins and reveal extensive heterogeneity, ranging from oligomannose-type glycans to highly-processed complex-type glycosylation. The structural mapping of glycans of trimeric S proteins revealed that some of these glycans contribute to the formation of a cluster of oligomannose-type glycans at specific regions of high glycan density on MERS-CoV S. Molecular evolution analysis of SARS and MERS S genes also reveals a higher incidence of amino-acid diversity on the exposed surfaces of the S proteins that are not occluded by N-linked glycans. In addition, we compare the structures of the respective glycan coats of SARS and HIV-1 envelope proteins using cryo-electron microscopy (cryo-EM) and computational modelling, which delineate a sparse glycan shield exhibited on SARS S compared with other viral glycoproteins. We therefore undertook a comparative analysis of viral glycan shields from characterized class I fusion proteins to highlight how glycosylation density influences oligomannose-type glycan abundance, and the relationship between effective glycan shields and viral evasion ability. Together, these data underscore the importance of glycosylation in viral immune evasion."}

{"project":"LitCovid-PD-FMA-UBERON","denotations":[{"id":"T27","span":{"begin":114,"end":127},"obj":"Body_part"},{"id":"T28","span":{"begin":299,"end":307},"obj":"Body_part"},{"id":"T29","span":{"begin":561,"end":571},"obj":"Body_part"},{"id":"T30","span":{"begin":615,"end":623},"obj":"Body_part"},{"id":"T31","span":{"begin":749,"end":752},"obj":"Body_part"},{"id":"T32","span":{"begin":764,"end":772},"obj":"Body_part"},{"id":"T33","span":{"begin":928,"end":941},"obj":"Body_part"},{"id":"T34","span":{"begin":1047,"end":1055},"obj":"Body_part"}],"attributes":[{"id":"A27","pred":"fma_id","subj":"T27","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A28","pred":"fma_id","subj":"T28","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A29","pred":"fma_id","subj":"T29","obj":"http://purl.org/sig/ont/fma/fma82739"},{"id":"A30","pred":"fma_id","subj":"T30","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A31","pred":"fma_id","subj":"T31","obj":"http://purl.org/sig/ont/fma/fma278683"},{"id":"A32","pred":"fma_id","subj":"T32","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A33","pred":"fma_id","subj":"T33","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A34","pred":"fma_id","subj":"T34","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"Here, we provide global and site-specific analyses of N-linked glycosylation on soluble SARS, MERS and HKU1 CoV S glycoproteins and reveal extensive heterogeneity, ranging from oligomannose-type glycans to highly-processed complex-type glycosylation. The structural mapping of glycans of trimeric S proteins revealed that some of these glycans contribute to the formation of a cluster of oligomannose-type glycans at specific regions of high glycan density on MERS-CoV S. Molecular evolution analysis of SARS and MERS S genes also reveals a higher incidence of amino-acid diversity on the exposed surfaces of the S proteins that are not occluded by N-linked glycans. In addition, we compare the structures of the respective glycan coats of SARS and HIV-1 envelope proteins using cryo-electron microscopy (cryo-EM) and computational modelling, which delineate a sparse glycan shield exhibited on SARS S compared with other viral glycoproteins. We therefore undertook a comparative analysis of viral glycan shields from characterized class I fusion proteins to highlight how glycosylation density influences oligomannose-type glycan abundance, and the relationship between effective glycan shields and viral evasion ability. Together, these data underscore the importance of glycosylation in viral immune evasion."}

{"project":"LitCovid-PD-MONDO","denotations":[{"id":"T19","span":{"begin":88,"end":92},"obj":"Disease"},{"id":"T20","span":{"begin":504,"end":508},"obj":"Disease"},{"id":"T21","span":{"begin":740,"end":744},"obj":"Disease"},{"id":"T22","span":{"begin":895,"end":899},"obj":"Disease"}],"attributes":[{"id":"A19","pred":"mondo_id","subj":"T19","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A20","pred":"mondo_id","subj":"T20","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A21","pred":"mondo_id","subj":"T21","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A22","pred":"mondo_id","subj":"T22","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"Here, we provide global and site-specific analyses of N-linked glycosylation on soluble SARS, MERS and HKU1 CoV S glycoproteins and reveal extensive heterogeneity, ranging from oligomannose-type glycans to highly-processed complex-type glycosylation. The structural mapping of glycans of trimeric S proteins revealed that some of these glycans contribute to the formation of a cluster of oligomannose-type glycans at specific regions of high glycan density on MERS-CoV S. Molecular evolution analysis of SARS and MERS S genes also reveals a higher incidence of amino-acid diversity on the exposed surfaces of the S proteins that are not occluded by N-linked glycans. In addition, we compare the structures of the respective glycan coats of SARS and HIV-1 envelope proteins using cryo-electron microscopy (cryo-EM) and computational modelling, which delineate a sparse glycan shield exhibited on SARS S compared with other viral glycoproteins. We therefore undertook a comparative analysis of viral glycan shields from characterized class I fusion proteins to highlight how glycosylation density influences oligomannose-type glycan abundance, and the relationship between effective glycan shields and viral evasion ability. Together, these data underscore the importance of glycosylation in viral immune evasion."}

{"project":"LitCovid-PD-CLO","denotations":[{"id":"T30","span":{"begin":375,"end":376},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T31","span":{"begin":520,"end":525},"obj":"http://purl.obolibrary.org/obo/OGG_0000000002"},{"id":"T32","span":{"begin":539,"end":540},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T33","span":{"begin":859,"end":860},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"},{"id":"T34","span":{"begin":966,"end":967},"obj":"http://purl.obolibrary.org/obo/CLO_0001020"}],"text":"Here, we provide global and site-specific analyses of N-linked glycosylation on soluble SARS, MERS and HKU1 CoV S glycoproteins and reveal extensive heterogeneity, ranging from oligomannose-type glycans to highly-processed complex-type glycosylation. The structural mapping of glycans of trimeric S proteins revealed that some of these glycans contribute to the formation of a cluster of oligomannose-type glycans at specific regions of high glycan density on MERS-CoV S. Molecular evolution analysis of SARS and MERS S genes also reveals a higher incidence of amino-acid diversity on the exposed surfaces of the S proteins that are not occluded by N-linked glycans. In addition, we compare the structures of the respective glycan coats of SARS and HIV-1 envelope proteins using cryo-electron microscopy (cryo-EM) and computational modelling, which delineate a sparse glycan shield exhibited on SARS S compared with other viral glycoproteins. We therefore undertook a comparative analysis of viral glycan shields from characterized class I fusion proteins to highlight how glycosylation density influences oligomannose-type glycan abundance, and the relationship between effective glycan shields and viral evasion ability. Together, these data underscore the importance of glycosylation in viral immune evasion."}

{"project":"LitCovid-PD-CHEBI","denotations":[{"id":"T30","span":{"begin":114,"end":127},"obj":"Chemical"},{"id":"T31","span":{"begin":195,"end":202},"obj":"Chemical"},{"id":"T32","span":{"begin":277,"end":284},"obj":"Chemical"},{"id":"T33","span":{"begin":299,"end":307},"obj":"Chemical"},{"id":"T34","span":{"begin":336,"end":343},"obj":"Chemical"},{"id":"T35","span":{"begin":406,"end":413},"obj":"Chemical"},{"id":"T36","span":{"begin":561,"end":566},"obj":"Chemical"},{"id":"T37","span":{"begin":567,"end":571},"obj":"Chemical"},{"id":"T38","span":{"begin":615,"end":623},"obj":"Chemical"},{"id":"T39","span":{"begin":658,"end":665},"obj":"Chemical"},{"id":"T40","span":{"begin":764,"end":772},"obj":"Chemical"},{"id":"T41","span":{"begin":784,"end":792},"obj":"Chemical"},{"id":"T42","span":{"begin":810,"end":812},"obj":"Chemical"},{"id":"T43","span":{"begin":928,"end":941},"obj":"Chemical"},{"id":"T44","span":{"begin":1047,"end":1055},"obj":"Chemical"}],"attributes":[{"id":"A30","pred":"chebi_id","subj":"T30","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A31","pred":"chebi_id","subj":"T31","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A32","pred":"chebi_id","subj":"T32","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A33","pred":"chebi_id","subj":"T33","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A34","pred":"chebi_id","subj":"T34","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A35","pred":"chebi_id","subj":"T35","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A36","pred":"chebi_id","subj":"T36","obj":"http://purl.obolibrary.org/obo/CHEBI_46882"},{"id":"A37","pred":"chebi_id","subj":"T37","obj":"http://purl.obolibrary.org/obo/CHEBI_37527"},{"id":"A38","pred":"chebi_id","subj":"T38","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A39","pred":"chebi_id","subj":"T39","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A40","pred":"chebi_id","subj":"T40","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A41","pred":"chebi_id","subj":"T41","obj":"http://purl.obolibrary.org/obo/CHEBI_10545"},{"id":"A42","pred":"chebi_id","subj":"T42","obj":"http://purl.obolibrary.org/obo/CHEBI_73507"},{"id":"A43","pred":"chebi_id","subj":"T43","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A44","pred":"chebi_id","subj":"T44","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"}],"text":"Here, we provide global and site-specific analyses of N-linked glycosylation on soluble SARS, MERS and HKU1 CoV S glycoproteins and reveal extensive heterogeneity, ranging from oligomannose-type glycans to highly-processed complex-type glycosylation. The structural mapping of glycans of trimeric S proteins revealed that some of these glycans contribute to the formation of a cluster of oligomannose-type glycans at specific regions of high glycan density on MERS-CoV S. Molecular evolution analysis of SARS and MERS S genes also reveals a higher incidence of amino-acid diversity on the exposed surfaces of the S proteins that are not occluded by N-linked glycans. In addition, we compare the structures of the respective glycan coats of SARS and HIV-1 envelope proteins using cryo-electron microscopy (cryo-EM) and computational modelling, which delineate a sparse glycan shield exhibited on SARS S compared with other viral glycoproteins. We therefore undertook a comparative analysis of viral glycan shields from characterized class I fusion proteins to highlight how glycosylation density influences oligomannose-type glycan abundance, and the relationship between effective glycan shields and viral evasion ability. Together, these data underscore the importance of glycosylation in viral immune evasion."}

{"project":"LitCovid-sample-MedDRA","denotations":[{"id":"T2","span":{"begin":793,"end":803},"obj":"http://purl.bioontology.org/ontology/MEDDRA/10022891"}],"attributes":[{"id":"A2","pred":"meddra_id","subj":"T2","obj":"http://purl.bioontology.org/ontology/MEDDRA/10069374"}],"text":"Here, we provide global and site-specific analyses of N-linked glycosylation on soluble SARS, MERS and HKU1 CoV S glycoproteins and reveal extensive heterogeneity, ranging from oligomannose-type glycans to highly-processed complex-type glycosylation. The structural mapping of glycans of trimeric S proteins revealed that some of these glycans contribute to the formation of a cluster of oligomannose-type glycans at specific regions of high glycan density on MERS-CoV S. Molecular evolution analysis of SARS and MERS S genes also reveals a higher incidence of amino-acid diversity on the exposed surfaces of the S proteins that are not occluded by N-linked glycans. In addition, we compare the structures of the respective glycan coats of SARS and HIV-1 envelope proteins using cryo-electron microscopy (cryo-EM) and computational modelling, which delineate a sparse glycan shield exhibited on SARS S compared with other viral glycoproteins. We therefore undertook a comparative analysis of viral glycan shields from characterized class I fusion proteins to highlight how glycosylation density influences oligomannose-type glycan abundance, and the relationship between effective glycan shields and viral evasion ability. Together, these data underscore the importance of glycosylation in viral immune evasion."}

{"project":"LitCovid-sample-PD-IDO","denotations":[{"id":"T20","span":{"begin":28,"end":32},"obj":"http://purl.obolibrary.org/obo/BFO_0000029"}],"text":"Here, we provide global and site-specific analyses of N-linked glycosylation on soluble SARS, MERS and HKU1 CoV S glycoproteins and reveal extensive heterogeneity, ranging from oligomannose-type glycans to highly-processed complex-type glycosylation. The structural mapping of glycans of trimeric S proteins revealed that some of these glycans contribute to the formation of a cluster of oligomannose-type glycans at specific regions of high glycan density on MERS-CoV S. Molecular evolution analysis of SARS and MERS S genes also reveals a higher incidence of amino-acid diversity on the exposed surfaces of the S proteins that are not occluded by N-linked glycans. In addition, we compare the structures of the respective glycan coats of SARS and HIV-1 envelope proteins using cryo-electron microscopy (cryo-EM) and computational modelling, which delineate a sparse glycan shield exhibited on SARS S compared with other viral glycoproteins. We therefore undertook a comparative analysis of viral glycan shields from characterized class I fusion proteins to highlight how glycosylation density influences oligomannose-type glycan abundance, and the relationship between effective glycan shields and viral evasion ability. Together, these data underscore the importance of glycosylation in viral immune evasion."}

{"project":"LitCovid-sample-Enju","denotations":[{"id":"T631","span":{"begin":0,"end":4},"obj":"RB"},{"id":"T632","span":{"begin":4,"end":5},"obj":"-COMMA-"},{"id":"T633","span":{"begin":6,"end":8},"obj":"PRP"},{"id":"T634","span":{"begin":9,"end":16},"obj":"VBP"},{"id":"T635","span":{"begin":17,"end":23},"obj":"JJ"},{"id":"T636","span":{"begin":24,"end":27},"obj":"CC"},{"id":"T637","span":{"begin":28,"end":41},"obj":"JJ"},{"id":"T638","span":{"begin":42,"end":50},"obj":"NNS"},{"id":"T639","span":{"begin":51,"end":53},"obj":"IN"},{"id":"T640","span":{"begin":54,"end":62},"obj":"JJ"},{"id":"T641","span":{"begin":63,"end":76},"obj":"NN"},{"id":"T642","span":{"begin":77,"end":79},"obj":"IN"},{"id":"T643","span":{"begin":80,"end":87},"obj":"JJ"},{"id":"T644","span":{"begin":88,"end":92},"obj":"NNS"},{"id":"T645","span":{"begin":92,"end":93},"obj":"-COMMA-"},{"id":"T646","span":{"begin":94,"end":98},"obj":"NNS"},{"id":"T647","span":{"begin":99,"end":102},"obj":"CC"},{"id":"T648","span":{"begin":103,"end":107},"obj":"NN"},{"id":"T649","span":{"begin":108,"end":111},"obj":"NN"},{"id":"T650","span":{"begin":112,"end":113},"obj":"NN"},{"id":"T651","span":{"begin":114,"end":127},"obj":"NNS"},{"id":"T652","span":{"begin":128,"end":131},"obj":"CC"},{"id":"T653","span":{"begin":132,"end":138},"obj":"VB"},{"id":"T654","span":{"begin":139,"end":148},"obj":"JJ"},{"id":"T655","span":{"begin":149,"end":162},"obj":"NN"},{"id":"T656","span":{"begin":162,"end":163},"obj":"-COMMA-"},{"id":"T657","span":{"begin":164,"end":171},"obj":"VBG"},{"id":"T658","span":{"begin":172,"end":176},"obj":"IN"},{"id":"T659","span":{"begin":177,"end":194},"obj":"JJ"},{"id":"T660","span":{"begin":195,"end":202},"obj":"NNS"},{"id":"T661","span":{"begin":203,"end":205},"obj":"TO"},{"id":"T662","span":{"begin":206,"end":222},"obj":"JJ"},{"id":"T663","span":{"begin":223,"end":235},"obj":"JJ"},{"id":"T664","span":{"begin":236,"end":249},"obj":"NN"},{"id":"T665","span":{"begin":251,"end":254},"obj":"DT"},{"id":"T666","span":{"begin":255,"end":265},"obj":"JJ"},{"id":"T667","span":{"begin":266,"end":273},"obj":"NN"},{"id":"T668","span":{"begin":274,"end":276},"obj":"IN"},{"id":"T669","span":{"begin":277,"end":284},"obj":"NNS"},{"id":"T670","span":{"begin":285,"end":287},"obj":"IN"},{"id":"T671","span":{"begin":288,"end":296},"obj":"JJ"},{"id":"T672","span":{"begin":297,"end":298},"obj":"NN"},{"id":"T673","span":{"begin":299,"end":307},"obj":"NNS"},{"id":"T674","span":{"begin":308,"end":316},"obj":"VBD"},{"id":"T675","span":{"begin":317,"end":321},"obj":"IN"},{"id":"T676","span":{"begin":322,"end":326},"obj":"DT"},{"id":"T677","span":{"begin":327,"end":329},"obj":"IN"},{"id":"T678","span":{"begin":330,"end":335},"obj":"DT"},{"id":"T679","span":{"begin":336,"end":343},"obj":"NNS"},{"id":"T680","span":{"begin":344,"end":354},"obj":"VBP"},{"id":"T681","span":{"begin":355,"end":357},"obj":"TO"},{"id":"T682","span":{"begin":358,"end":361},"obj":"DT"},{"id":"T683","span":{"begin":362,"end":371},"obj":"NN"},{"id":"T684","span":{"begin":372,"end":374},"obj":"IN"},{"id":"T685","span":{"begin":375,"end":376},"obj":"DT"},{"id":"T686","span":{"begin":377,"end":384},"obj":"NN"},{"id":"T687","span":{"begin":385,"end":387},"obj":"IN"},{"id":"T688","span":{"begin":388,"end":405},"obj":"JJ"},{"id":"T689","span":{"begin":406,"end":413},"obj":"NNS"},{"id":"T690","span":{"begin":414,"end":416},"obj":"IN"},{"id":"T691","span":{"begin":417,"end":425},"obj":"JJ"},{"id":"T692","span":{"begin":426,"end":433},"obj":"NNS"},{"id":"T693","span":{"begin":434,"end":436},"obj":"IN"},{"id":"T694","span":{"begin":437,"end":441},"obj":"JJ"},{"id":"T695","span":{"begin":442,"end":448},"obj":"NN"},{"id":"T696","span":{"begin":449,"end":456},"obj":"NN"},{"id":"T697","span":{"begin":457,"end":459},"obj":"IN"},{"id":"T698","span":{"begin":460,"end":468},"obj":"NNP"},{"id":"T699","span":{"begin":469,"end":471},"obj":"NNP"},{"id":"T700","span":{"begin":472,"end":481},"obj":"NNP"},{"id":"T701","span":{"begin":482,"end":491},"obj":"NN"},{"id":"T702","span":{"begin":492,"end":500},"obj":"NN"},{"id":"T703","span":{"begin":501,"end":503},"obj":"IN"},{"id":"T704","span":{"begin":504,"end":508},"obj":"NNP"},{"id":"T705","span":{"begin":509,"end":512},"obj":"CC"},{"id":"T706","span":{"begin":513,"end":517},"obj":"NNP"},{"id":"T707","span":{"begin":518,"end":519},"obj":"NN"},{"id":"T708","span":{"begin":520,"end":525},"obj":"NNS"},{"id":"T709","span":{"begin":526,"end":530},"obj":"RB"},{"id":"T710","span":{"begin":531,"end":538},"obj":"VBZ"},{"id":"T711","span":{"begin":539,"end":540},"obj":"DT"},{"id":"T712","span":{"begin":541,"end":547},"obj":"JJR"},{"id":"T713","span":{"begin":548,"end":557},"obj":"NN"},{"id":"T714","span":{"begin":558,"end":560},"obj":"IN"},{"id":"T715","span":{"begin":561,"end":571},"obj":"JJ"},{"id":"T716","span":{"begin":572,"end":581},"obj":"NN"},{"id":"T717","span":{"begin":582,"end":584},"obj":"IN"},{"id":"T718","span":{"begin":585,"end":588},"obj":"DT"},{"id":"T719","span":{"begin":589,"end":596},"obj":"VBN"},{"id":"T720","span":{"begin":597,"end":605},"obj":"NNS"},{"id":"T721","span":{"begin":606,"end":608},"obj":"IN"},{"id":"T722","span":{"begin":609,"end":612},"obj":"DT"},{"id":"T723","span":{"begin":613,"end":614},"obj":"NN"},{"id":"T724","span":{"begin":615,"end":623},"obj":"NNS"},{"id":"T725","span":{"begin":624,"end":628},"obj":"WDT"},{"id":"T726","span":{"begin":629,"end":632},"obj":"VBP"},{"id":"T727","span":{"begin":633,"end":636},"obj":"RB"},{"id":"T728","span":{"begin":637,"end":645},"obj":"VBN"},{"id":"T729","span":{"begin":646,"end":648},"obj":"IN"},{"id":"T730","span":{"begin":649,"end":657},"obj":"JJ"},{"id":"T731","span":{"begin":658,"end":665},"obj":"NNS"},{"id":"T732","span":{"begin":667,"end":669},"obj":"IN"},{"id":"T733","span":{"begin":670,"end":678},"obj":"NN"},{"id":"T734","span":{"begin":678,"end":679},"obj":"-COMMA-"},{"id":"T735","span":{"begin":680,"end":682},"obj":"PRP"},{"id":"T736","span":{"begin":683,"end":690},"obj":"VBP"},{"id":"T737","span":{"begin":691,"end":694},"obj":"DT"},{"id":"T738","span":{"begin":695,"end":705},"obj":"NNS"},{"id":"T739","span":{"begin":706,"end":708},"obj":"IN"},{"id":"T740","span":{"begin":709,"end":712},"obj":"DT"},{"id":"T741","span":{"begin":713,"end":723},"obj":"JJ"},{"id":"T742","span":{"begin":724,"end":730},"obj":"NN"},{"id":"T743","span":{"begin":731,"end":736},"obj":"NNS"},{"id":"T744","span":{"begin":737,"end":739},"obj":"IN"},{"id":"T745","span":{"begin":740,"end":744},"obj":"NN"},{"id":"T746","span":{"begin":745,"end":748},"obj":"CC"},{"id":"T747","span":{"begin":749,"end":754},"obj":"NN"},{"id":"T748","span":{"begin":755,"end":763},"obj":"NN"},{"id":"T749","span":{"begin":764,"end":772},"obj":"NNS"},{"id":"T750","span":{"begin":773,"end":778},"obj":"VBG"},{"id":"T751","span":{"begin":779,"end":792},"obj":"NN"},{"id":"T752","span":{"begin":793,"end":803},"obj":"NN"},{"id":"T753","span":{"begin":804,"end":805},"obj":"-LRB-"},{"id":"T754","span":{"begin":805,"end":812},"obj":"NN"},{"id":"T755","span":{"begin":812,"end":813},"obj":"-RRB-"},{"id":"T756","span":{"begin":814,"end":817},"obj":"CC"},{"id":"T757","span":{"begin":818,"end":831},"obj":"JJ"},{"id":"T758","span":{"begin":832,"end":841},"obj":"NN"},{"id":"T759","span":{"begin":841,"end":842},"obj":"-COMMA-"},{"id":"T760","span":{"begin":843,"end":848},"obj":"WDT"},{"id":"T761","span":{"begin":849,"end":858},"obj":"VBP"},{"id":"T762","span":{"begin":859,"end":860},"obj":"DT"},{"id":"T763","span":{"begin":861,"end":867},"obj":"JJ"},{"id":"T764","span":{"begin":868,"end":874},"obj":"NN"},{"id":"T765","span":{"begin":875,"end":881},"obj":"NN"},{"id":"T766","span":{"begin":882,"end":891},"obj":"VBD"},{"id":"T767","span":{"begin":892,"end":894},"obj":"IN"},{"id":"T768","span":{"begin":895,"end":899},"obj":"NNP"},{"id":"T769","span":{"begin":900,"end":901},"obj":"NN"},{"id":"T770","span":{"begin":902,"end":910},"obj":"VBN"},{"id":"T771","span":{"begin":911,"end":915},"obj":"IN"},{"id":"T772","span":{"begin":916,"end":921},"obj":"JJ"},{"id":"T773","span":{"begin":922,"end":927},"obj":"JJ"},{"id":"T774","span":{"begin":928,"end":941},"obj":"NNS"},{"id":"T775","span":{"begin":943,"end":945},"obj":"PRP"},{"id":"T776","span":{"begin":946,"end":955},"obj":"RB"},{"id":"T777","span":{"begin":956,"end":965},"obj":"VBD"},{"id":"T778","span":{"begin":966,"end":967},"obj":"DT"},{"id":"T779","span":{"begin":968,"end":979},"obj":"JJ"},{"id":"T780","span":{"begin":980,"end":988},"obj":"NN"},{"id":"T781","span":{"begin":989,"end":991},"obj":"IN"},{"id":"T782","span":{"begin":992,"end":997},"obj":"JJ"},{"id":"T783","span":{"begin":998,"end":1004},"obj":"NN"},{"id":"T784","span":{"begin":1005,"end":1012},"obj":"NNS"},{"id":"T785","span":{"begin":1013,"end":1017},"obj":"IN"},{"id":"T786","span":{"begin":1018,"end":1031},"obj":"VBN"},{"id":"T787","span":{"begin":1032,"end":1037},"obj":"NN"},{"id":"T788","span":{"begin":1038,"end":1039},"obj":"CD"},{"id":"T789","span":{"begin":1040,"end":1046},"obj":"NN"},{"id":"T790","span":{"begin":1047,"end":1055},"obj":"NNS"},{"id":"T791","span":{"begin":1056,"end":1058},"obj":"TO"},{"id":"T792","span":{"begin":1059,"end":1068},"obj":"VB"},{"id":"T793","span":{"begin":1069,"end":1072},"obj":"WRB"},{"id":"T794","span":{"begin":1073,"end":1086},"obj":"NN"},{"id":"T795","span":{"begin":1087,"end":1094},"obj":"NN"},{"id":"T796","span":{"begin":1095,"end":1105},"obj":"VBZ"},{"id":"T797","span":{"begin":1106,"end":1123},"obj":"JJ"},{"id":"T798","span":{"begin":1124,"end":1130},"obj":"NN"},{"id":"T799","span":{"begin":1131,"end":1140},"obj":"NN"},{"id":"T800","span":{"begin":1140,"end":1141},"obj":"-COMMA-"},{"id":"T801","span":{"begin":1142,"end":1145},"obj":"CC"},{"id":"T802","span":{"begin":1146,"end":1149},"obj":"DT"},{"id":"T803","span":{"begin":1150,"end":1162},"obj":"NN"},{"id":"T804","span":{"begin":1163,"end":1170},"obj":"IN"},{"id":"T805","span":{"begin":1171,"end":1180},"obj":"JJ"},{"id":"T806","span":{"begin":1181,"end":1187},"obj":"NN"},{"id":"T807","span":{"begin":1188,"end":1195},"obj":"NNS"},{"id":"T808","span":{"begin":1196,"end":1199},"obj":"CC"},{"id":"T809","span":{"begin":1200,"end":1205},"obj":"JJ"},{"id":"T810","span":{"begin":1206,"end":1213},"obj":"NN"},{"id":"T811","span":{"begin":1214,"end":1221},"obj":"NN"},{"id":"T812","span":{"begin":1223,"end":1231},"obj":"RB"},{"id":"T813","span":{"begin":1231,"end":1232},"obj":"-COMMA-"},{"id":"T814","span":{"begin":1233,"end":1238},"obj":"DT"},{"id":"T815","span":{"begin":1239,"end":1243},"obj":"NNS"},{"id":"T816","span":{"begin":1244,"end":1254},"obj":"VBP"},{"id":"T817","span":{"begin":1255,"end":1258},"obj":"DT"},{"id":"T818","span":{"begin":1259,"end":1269},"obj":"NN"},{"id":"T819","span":{"begin":1270,"end":1272},"obj":"IN"},{"id":"T820","span":{"begin":1273,"end":1286},"obj":"NN"},{"id":"T821","span":{"begin":1287,"end":1289},"obj":"IN"},{"id":"T822","span":{"begin":1290,"end":1295},"obj":"JJ"},{"id":"T823","span":{"begin":1296,"end":1302},"obj":"JJ"},{"id":"T824","span":{"begin":1303,"end":1310},"obj":"NN"}],"relations":[{"id":"R635","pred":"arg1Of","subj":"T652","obj":"T631"},{"id":"R636","pred":"arg1Of","subj":"T652","obj":"T632"},{"id":"R637","pred":"arg1Of","subj":"T633","obj":"T634"},{"id":"R638","pred":"arg2Of","subj":"T638","obj":"T634"},{"id":"R639","pred":"arg1Of","subj":"T638","obj":"T635"},{"id":"R640","pred":"arg1Of","subj":"T635","obj":"T636"},{"id":"R641","pred":"arg2Of","subj":"T637","obj":"T636"},{"id":"R642","pred":"arg1Of","subj":"T638","obj":"T637"},{"id":"R643","pred":"arg1Of","subj":"T638","obj":"T639"},{"id":"R644","pred":"arg2Of","subj":"T641","obj":"T639"},{"id":"R645","pred":"arg1Of","subj":"T641","obj":"T640"},{"id":"R646","pred":"arg1Of","subj":"T634","obj":"T642"},{"id":"R647","pred":"arg2Of","subj":"T647","obj":"T642"},{"id":"R648","pred":"arg1Of","subj":"T644","obj":"T643"},{"id":"R649","pred":"arg1Of","subj":"T644","obj":"T645"},{"id":"R650","pred":"arg2Of","subj":"T646","obj":"T645"},{"id":"R651","pred":"arg1Of","subj":"T645","obj":"T647"},{"id":"R652","pred":"arg2Of","subj":"T651","obj":"T647"},{"id":"R653","pred":"arg1Of","subj":"T651","obj":"T648"},{"id":"R654","pred":"arg1Of","subj":"T651","obj":"T649"},{"id":"R655","pred":"arg1Of","subj":"T651","obj":"T650"},{"id":"R656","pred":"arg1Of","subj":"T634","obj":"T652"},{"id":"R657","pred":"arg2Of","subj":"T653","obj":"T652"},{"id":"R658","pred":"arg1Of","subj":"T633","obj":"T653"},{"id":"R659","pred":"arg2Of","subj":"T655","obj":"T653"},{"id":"R660","pred":"arg1Of","subj":"T655","obj":"T654"},{"id":"R661","pred":"arg1Of","subj":"T655","obj":"T656"},{"id":"R662","pred":"arg1Of","subj":"T655","obj":"T657"},{"id":"R663","pred":"arg1Of","subj":"T657","obj":"T658"},{"id":"R664","pred":"arg2Of","subj":"T660","obj":"T658"},{"id":"R665","pred":"arg1Of","subj":"T660","obj":"T659"},{"id":"R666","pred":"arg1Of","subj":"T655","obj":"T661"},{"id":"R667","pred":"arg2Of","subj":"T664","obj":"T661"},{"id":"R668","pred":"arg1Of","subj":"T664","obj":"T662"},{"id":"R669","pred":"arg1Of","subj":"T664","obj":"T663"},{"id":"R670","pred":"arg1Of","subj":"T667","obj":"T665"},{"id":"R671","pred":"arg1Of","subj":"T667","obj":"T666"},{"id":"R672","pred":"arg1Of","subj":"T667","obj":"T668"},{"id":"R673","pred":"arg2Of","subj":"T669","obj":"T668"},{"id":"R674","pred":"arg1Of","subj":"T669","obj":"T670"},{"id":"R675","pred":"arg2Of","subj":"T673","obj":"T670"},{"id":"R676","pred":"arg1Of","subj":"T673","obj":"T671"},{"id":"R677","pred":"arg1Of","subj":"T673","obj":"T672"},{"id":"R678","pred":"arg1Of","subj":"T667","obj":"T674"},{"id":"R679","pred":"arg2Of","subj":"T680","obj":"T674"},{"id":"R680","pred":"arg1Of","subj":"T680","obj":"T675"},{"id":"R681","pred":"arg1Of","subj":"T676","obj":"T677"},{"id":"R682","pred":"arg2Of","subj":"T679","obj":"T677"},{"id":"R683","pred":"arg1Of","subj":"T679","obj":"T678"},{"id":"R684","pred":"arg1Of","subj":"T676","obj":"T680"},{"id":"R685","pred":"arg1Of","subj":"T680","obj":"T681"},{"id":"R686","pred":"arg2Of","subj":"T683","obj":"T681"},{"id":"R687","pred":"arg1Of","subj":"T683","obj":"T682"},{"id":"R688","pred":"arg1Of","subj":"T683","obj":"T684"},{"id":"R689","pred":"arg2Of","subj":"T686","obj":"T684"},{"id":"R690","pred":"arg1Of","subj":"T686","obj":"T685"},{"id":"R691","pred":"arg1Of","subj":"T686","obj":"T687"},{"id":"R692","pred":"arg2Of","subj":"T689","obj":"T687"},{"id":"R693","pred":"arg1Of","subj":"T689","obj":"T688"},{"id":"R694","pred":"arg1Of","subj":"T680","obj":"T690"},{"id":"R695","pred":"arg2Of","subj":"T692","obj":"T690"},{"id":"R696","pred":"arg1Of","subj":"T692","obj":"T691"},{"id":"R697","pred":"arg1Of","subj":"T692","obj":"T693"},{"id":"R698","pred":"arg2Of","subj":"T696","obj":"T693"},{"id":"R699","pred":"arg1Of","subj":"T696","obj":"T694"},{"id":"R700","pred":"arg1Of","subj":"T696","obj":"T695"},{"id":"R701","pred":"arg1Of","subj":"T680","obj":"T697"},{"id":"R702","pred":"arg2Of","subj":"T710","obj":"T697"},{"id":"R703","pred":"arg1Of","subj":"T700","obj":"T698"},{"id":"R704","pred":"arg1Of","subj":"T700","obj":"T699"},{"id":"R705","pred":"arg1Of","subj":"T702","obj":"T700"},{"id":"R706","pred":"arg1Of","subj":"T702","obj":"T701"},{"id":"R707","pred":"arg1Of","subj":"T702","obj":"T703"},{"id":"R708","pred":"arg2Of","subj":"T708","obj":"T703"},{"id":"R709","pred":"arg1Of","subj":"T708","obj":"T704"},{"id":"R710","pred":"arg1Of","subj":"T704","obj":"T705"},{"id":"R711","pred":"arg2Of","subj":"T706","obj":"T705"},{"id":"R712","pred":"arg1Of","subj":"T708","obj":"T706"},{"id":"R713","pred":"arg1Of","subj":"T708","obj":"T707"},{"id":"R714","pred":"arg1Of","subj":"T710","obj":"T709"},{"id":"R715","pred":"arg1Of","subj":"T702","obj":"T710"},{"id":"R716","pred":"arg2Of","subj":"T713","obj":"T710"},{"id":"R717","pred":"arg1Of","subj":"T713","obj":"T711"},{"id":"R718","pred":"arg1Of","subj":"T713","obj":"T712"},{"id":"R719","pred":"arg1Of","subj":"T713","obj":"T714"},{"id":"R720","pred":"arg2Of","subj":"T716","obj":"T714"},{"id":"R721","pred":"arg1Of","subj":"T716","obj":"T715"},{"id":"R722","pred":"arg1Of","subj":"T710","obj":"T717"},{"id":"R723","pred":"arg2Of","subj":"T720","obj":"T717"},{"id":"R724","pred":"arg1Of","subj":"T720","obj":"T718"},{"id":"R725","pred":"arg2Of","subj":"T720","obj":"T719"},{"id":"R726","pred":"arg1Of","subj":"T720","obj":"T721"},{"id":"R727","pred":"arg2Of","subj":"T724","obj":"T721"},{"id":"R728","pred":"arg1Of","subj":"T724","obj":"T722"},{"id":"R729","pred":"arg1Of","subj":"T724","obj":"T723"},{"id":"R730","pred":"arg1Of","subj":"T720","obj":"T725"},{"id":"R731","pred":"arg1Of","subj":"T720","obj":"T726"},{"id":"R732","pred":"arg2Of","subj":"T728","obj":"T726"},{"id":"R733","pred":"arg1Of","subj":"T728","obj":"T727"},{"id":"R734","pred":"arg1Of","subj":"T731","obj":"T728"},{"id":"R735","pred":"arg2Of","subj":"T720","obj":"T728"},{"id":"R736","pred":"arg2Of","subj":"T731","obj":"T729"},{"id":"R737","pred":"arg1Of","subj":"T731","obj":"T730"},{"id":"R738","pred":"arg1Of","subj":"T746","obj":"T732"},{"id":"R739","pred":"arg2Of","subj":"T733","obj":"T732"},{"id":"R740","pred":"arg1Of","subj":"T746","obj":"T734"},{"id":"R741","pred":"arg1Of","subj":"T735","obj":"T736"},{"id":"R742","pred":"arg2Of","subj":"T738","obj":"T736"},{"id":"R743","pred":"arg1Of","subj":"T738","obj":"T737"},{"id":"R744","pred":"arg1Of","subj":"T738","obj":"T739"},{"id":"R745","pred":"arg2Of","subj":"T743","obj":"T739"},{"id":"R746","pred":"arg1Of","subj":"T743","obj":"T740"},{"id":"R747","pred":"arg1Of","subj":"T743","obj":"T741"},{"id":"R748","pred":"arg1Of","subj":"T743","obj":"T742"},{"id":"R749","pred":"arg1Of","subj":"T743","obj":"T744"},{"id":"R750","pred":"arg2Of","subj":"T745","obj":"T744"},{"id":"R751","pred":"arg1Of","subj":"T736","obj":"T746"},{"id":"R752","pred":"arg2Of","subj":"T766","obj":"T746"},{"id":"R753","pred":"arg1Of","subj":"T749","obj":"T747"},{"id":"R754","pred":"arg1Of","subj":"T749","obj":"T748"},{"id":"R755","pred":"arg1Of","subj":"T749","obj":"T750"},{"id":"R756","pred":"arg2Of","subj":"T756","obj":"T750"},{"id":"R757","pred":"arg1Of","subj":"T752","obj":"T751"},{"id":"R758","pred":"arg1Of","subj":"T752","obj":"T753"},{"id":"R759","pred":"arg2Of","subj":"T754","obj":"T753"},{"id":"R760","pred":"arg3Of","subj":"T755","obj":"T753"},{"id":"R761","pred":"arg1Of","subj":"T752","obj":"T756"},{"id":"R762","pred":"arg2Of","subj":"T758","obj":"T756"},{"id":"R763","pred":"arg1Of","subj":"T758","obj":"T757"},{"id":"R764","pred":"arg1Of","subj":"T758","obj":"T759"},{"id":"R765","pred":"arg1Of","subj":"T758","obj":"T760"},{"id":"R766","pred":"arg1Of","subj":"T758","obj":"T761"},{"id":"R767","pred":"arg2Of","subj":"T765","obj":"T761"},{"id":"R768","pred":"arg1Of","subj":"T765","obj":"T762"},{"id":"R769","pred":"arg1Of","subj":"T765","obj":"T763"},{"id":"R770","pred":"arg1Of","subj":"T765","obj":"T764"},{"id":"R771","pred":"arg1Of","subj":"T749","obj":"T766"},{"id":"R772","pred":"arg2Of","subj":"T769","obj":"T766"},{"id":"R773","pred":"arg1Of","subj":"T766","obj":"T767"},{"id":"R774","pred":"arg2Of","subj":"T768","obj":"T767"},{"id":"R775","pred":"arg1Of","subj":"T766","obj":"T770"},{"id":"R776","pred":"arg2Of","subj":"T771","obj":"T770"},{"id":"R777","pred":"arg2Of","subj":"T774","obj":"T771"},{"id":"R778","pred":"arg1Of","subj":"T774","obj":"T772"},{"id":"R779","pred":"arg1Of","subj":"T774","obj":"T773"},{"id":"R780","pred":"arg1Of","subj":"T777","obj":"T776"},{"id":"R781","pred":"arg1Of","subj":"T775","obj":"T777"},{"id":"R782","pred":"arg2Of","subj":"T780","obj":"T777"},{"id":"R783","pred":"arg1Of","subj":"T780","obj":"T778"},{"id":"R784","pred":"arg1Of","subj":"T780","obj":"T779"},{"id":"R785","pred":"arg1Of","subj":"T780","obj":"T781"},{"id":"R786","pred":"arg2Of","subj":"T801","obj":"T781"},{"id":"R787","pred":"arg1Of","subj":"T784","obj":"T782"},{"id":"R788","pred":"arg1Of","subj":"T784","obj":"T783"},{"id":"R789","pred":"arg1Of","subj":"T784","obj":"T785"},{"id":"R790","pred":"arg2Of","subj":"T790","obj":"T785"},{"id":"R791","pred":"arg2Of","subj":"T790","obj":"T786"},{"id":"R792","pred":"arg1Of","subj":"T790","obj":"T787"},{"id":"R793","pred":"arg1Of","subj":"T790","obj":"T788"},{"id":"R794","pred":"arg1Of","subj":"T790","obj":"T789"},{"id":"R795","pred":"arg1Of","subj":"T792","obj":"T791"},{"id":"R796","pred":"modOf","subj":"T784","obj":"T791"},{"id":"R797","pred":"arg2Of","subj":"T793","obj":"T792"},{"id":"R798","pred":"arg1Of","subj":"T796","obj":"T793"},{"id":"R799","pred":"arg1Of","subj":"T795","obj":"T794"},{"id":"R800","pred":"arg1Of","subj":"T795","obj":"T796"},{"id":"R801","pred":"arg2Of","subj":"T799","obj":"T796"},{"id":"R802","pred":"arg1Of","subj":"T799","obj":"T797"},{"id":"R803","pred":"arg1Of","subj":"T799","obj":"T798"},{"id":"R804","pred":"arg1Of","subj":"T801","obj":"T800"},{"id":"R805","pred":"arg1Of","subj":"T784","obj":"T801"},{"id":"R806","pred":"arg2Of","subj":"T803","obj":"T801"},{"id":"R807","pred":"arg1Of","subj":"T803","obj":"T802"},{"id":"R808","pred":"arg1Of","subj":"T803","obj":"T804"},{"id":"R809","pred":"arg2Of","subj":"T808","obj":"T804"},{"id":"R810","pred":"arg1Of","subj":"T807","obj":"T805"},{"id":"R811","pred":"arg1Of","subj":"T807","obj":"T806"},{"id":"R812","pred":"arg1Of","subj":"T807","obj":"T808"},{"id":"R813","pred":"arg2Of","subj":"T811","obj":"T808"},{"id":"R814","pred":"arg1Of","subj":"T811","obj":"T809"},{"id":"R815","pred":"arg1Of","subj":"T811","obj":"T810"},{"id":"R816","pred":"arg1Of","subj":"T816","obj":"T812"},{"id":"R817","pred":"arg1Of","subj":"T816","obj":"T813"},{"id":"R818","pred":"arg1Of","subj":"T815","obj":"T814"},{"id":"R819","pred":"arg1Of","subj":"T815","obj":"T816"},{"id":"R820","pred":"arg2Of","subj":"T818","obj":"T816"},{"id":"R821","pred":"arg1Of","subj":"T818","obj":"T817"},{"id":"R822","pred":"arg1Of","subj":"T818","obj":"T819"},{"id":"R823","pred":"arg2Of","subj":"T820","obj":"T819"},{"id":"R824","pred":"arg1Of","subj":"T818","obj":"T821"},{"id":"R825","pred":"arg2Of","subj":"T824","obj":"T821"},{"id":"R826","pred":"arg1Of","subj":"T824","obj":"T822"},{"id":"R827","pred":"arg1Of","subj":"T824","obj":"T823"}],"text":"Here, we provide global and site-specific analyses of N-linked glycosylation on soluble SARS, MERS and HKU1 CoV S glycoproteins and reveal extensive heterogeneity, ranging from oligomannose-type glycans to highly-processed complex-type glycosylation. The structural mapping of glycans of trimeric S proteins revealed that some of these glycans contribute to the formation of a cluster of oligomannose-type glycans at specific regions of high glycan density on MERS-CoV S. Molecular evolution analysis of SARS and MERS S genes also reveals a higher incidence of amino-acid diversity on the exposed surfaces of the S proteins that are not occluded by N-linked glycans. In addition, we compare the structures of the respective glycan coats of SARS and HIV-1 envelope proteins using cryo-electron microscopy (cryo-EM) and computational modelling, which delineate a sparse glycan shield exhibited on SARS S compared with other viral glycoproteins. We therefore undertook a comparative analysis of viral glycan shields from characterized class I fusion proteins to highlight how glycosylation density influences oligomannose-type glycan abundance, and the relationship between effective glycan shields and viral evasion ability. Together, these data underscore the importance of glycosylation in viral immune evasion."}

{"project":"LitCovid-sample-PD-FMA","denotations":[{"id":"T27","span":{"begin":114,"end":127},"obj":"Body_part"},{"id":"T28","span":{"begin":299,"end":307},"obj":"Body_part"},{"id":"T29","span":{"begin":561,"end":571},"obj":"Body_part"},{"id":"T30","span":{"begin":615,"end":623},"obj":"Body_part"},{"id":"T31","span":{"begin":749,"end":752},"obj":"Body_part"},{"id":"T32","span":{"begin":764,"end":772},"obj":"Body_part"},{"id":"T33","span":{"begin":928,"end":941},"obj":"Body_part"},{"id":"T34","span":{"begin":1047,"end":1055},"obj":"Body_part"}],"attributes":[{"id":"A27","pred":"fma_id","subj":"T27","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A28","pred":"fma_id","subj":"T28","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A29","pred":"fma_id","subj":"T29","obj":"http://purl.org/sig/ont/fma/fma82739"},{"id":"A30","pred":"fma_id","subj":"T30","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A31","pred":"fma_id","subj":"T31","obj":"http://purl.org/sig/ont/fma/fma278683"},{"id":"A32","pred":"fma_id","subj":"T32","obj":"http://purl.org/sig/ont/fma/fma67257"},{"id":"A33","pred":"fma_id","subj":"T33","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A34","pred":"fma_id","subj":"T34","obj":"http://purl.org/sig/ont/fma/fma67257"}],"text":"Here, we provide global and site-specific analyses of N-linked glycosylation on soluble SARS, MERS and HKU1 CoV S glycoproteins and reveal extensive heterogeneity, ranging from oligomannose-type glycans to highly-processed complex-type glycosylation. The structural mapping of glycans of trimeric S proteins revealed that some of these glycans contribute to the formation of a cluster of oligomannose-type glycans at specific regions of high glycan density on MERS-CoV S. Molecular evolution analysis of SARS and MERS S genes also reveals a higher incidence of amino-acid diversity on the exposed surfaces of the S proteins that are not occluded by N-linked glycans. In addition, we compare the structures of the respective glycan coats of SARS and HIV-1 envelope proteins using cryo-electron microscopy (cryo-EM) and computational modelling, which delineate a sparse glycan shield exhibited on SARS S compared with other viral glycoproteins. We therefore undertook a comparative analysis of viral glycan shields from characterized class I fusion proteins to highlight how glycosylation density influences oligomannose-type glycan abundance, and the relationship between effective glycan shields and viral evasion ability. Together, these data underscore the importance of glycosylation in viral immune evasion."}

{"project":"LitCovid-sample-CHEBI","denotations":[{"id":"T26","span":{"begin":114,"end":127},"obj":"Chemical"},{"id":"T27","span":{"begin":195,"end":202},"obj":"Chemical"},{"id":"T28","span":{"begin":277,"end":284},"obj":"Chemical"},{"id":"T29","span":{"begin":299,"end":307},"obj":"Chemical"},{"id":"T30","span":{"begin":336,"end":343},"obj":"Chemical"},{"id":"T31","span":{"begin":406,"end":413},"obj":"Chemical"},{"id":"T32","span":{"begin":561,"end":566},"obj":"Chemical"},{"id":"T33","span":{"begin":615,"end":623},"obj":"Chemical"},{"id":"T34","span":{"begin":658,"end":665},"obj":"Chemical"},{"id":"T35","span":{"begin":764,"end":772},"obj":"Chemical"},{"id":"T36","span":{"begin":928,"end":941},"obj":"Chemical"},{"id":"T37","span":{"begin":1047,"end":1055},"obj":"Chemical"}],"attributes":[{"id":"A27","pred":"chebi_id","subj":"T27","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A34","pred":"chebi_id","subj":"T34","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A26","pred":"chebi_id","subj":"T26","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A37","pred":"chebi_id","subj":"T37","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A36","pred":"chebi_id","subj":"T36","obj":"http://purl.obolibrary.org/obo/CHEBI_17089"},{"id":"A28","pred":"chebi_id","subj":"T28","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A33","pred":"chebi_id","subj":"T33","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A32","pred":"chebi_id","subj":"T32","obj":"http://purl.obolibrary.org/obo/CHEBI_46882"},{"id":"A31","pred":"chebi_id","subj":"T31","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A35","pred":"chebi_id","subj":"T35","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"},{"id":"A30","pred":"chebi_id","subj":"T30","obj":"http://purl.obolibrary.org/obo/CHEBI_18154"},{"id":"A29","pred":"chebi_id","subj":"T29","obj":"http://purl.obolibrary.org/obo/CHEBI_36080"}],"text":"Here, we provide global and site-specific analyses of N-linked glycosylation on soluble SARS, MERS and HKU1 CoV S glycoproteins and reveal extensive heterogeneity, ranging from oligomannose-type glycans to highly-processed complex-type glycosylation. The structural mapping of glycans of trimeric S proteins revealed that some of these glycans contribute to the formation of a cluster of oligomannose-type glycans at specific regions of high glycan density on MERS-CoV S. Molecular evolution analysis of SARS and MERS S genes also reveals a higher incidence of amino-acid diversity on the exposed surfaces of the S proteins that are not occluded by N-linked glycans. In addition, we compare the structures of the respective glycan coats of SARS and HIV-1 envelope proteins using cryo-electron microscopy (cryo-EM) and computational modelling, which delineate a sparse glycan shield exhibited on SARS S compared with other viral glycoproteins. We therefore undertook a comparative analysis of viral glycan shields from characterized class I fusion proteins to highlight how glycosylation density influences oligomannose-type glycan abundance, and the relationship between effective glycan shields and viral evasion ability. Together, these data underscore the importance of glycosylation in viral immune evasion."}

{"project":"LitCovid-sample-PD-NCBITaxon","denotations":[{"id":"T31","span":{"begin":88,"end":92},"obj":"Species"},{"id":"T32","span":{"begin":94,"end":98},"obj":"Species"},{"id":"T33","span":{"begin":103,"end":111},"obj":"Species"},{"id":"T34","span":{"begin":460,"end":468},"obj":"Species"},{"id":"T35","span":{"begin":504,"end":508},"obj":"Species"},{"id":"T36","span":{"begin":513,"end":517},"obj":"Species"},{"id":"T37","span":{"begin":740,"end":744},"obj":"Species"},{"id":"T38","span":{"begin":749,"end":754},"obj":"Species"},{"id":"T39","span":{"begin":895,"end":899},"obj":"Species"}],"attributes":[{"id":"A31","pred":"ncbi_taxonomy_id","subj":"T31","obj":"NCBItxid:694009"},{"id":"A32","pred":"ncbi_taxonomy_id","subj":"T32","obj":"NCBItxid:1335626"},{"id":"A33","pred":"ncbi_taxonomy_id","subj":"T33","obj":"NCBItxid:290028"},{"id":"A34","pred":"ncbi_taxonomy_id","subj":"T34","obj":"NCBItxid:1335626"},{"id":"A35","pred":"ncbi_taxonomy_id","subj":"T35","obj":"NCBItxid:694009"},{"id":"A36","pred":"ncbi_taxonomy_id","subj":"T36","obj":"NCBItxid:1335626"},{"id":"A37","pred":"ncbi_taxonomy_id","subj":"T37","obj":"NCBItxid:694009"},{"id":"A38","pred":"ncbi_taxonomy_id","subj":"T38","obj":"NCBItxid:11676"},{"id":"A39","pred":"ncbi_taxonomy_id","subj":"T39","obj":"NCBItxid:694009"}],"namespaces":[{"prefix":"NCBItxid","uri":"http://purl.bioontology.org/ontology/NCBITAXON/"}],"text":"Here, we provide global and site-specific analyses of N-linked glycosylation on soluble SARS, MERS and HKU1 CoV S glycoproteins and reveal extensive heterogeneity, ranging from oligomannose-type glycans to highly-processed complex-type glycosylation. The structural mapping of glycans of trimeric S proteins revealed that some of these glycans contribute to the formation of a cluster of oligomannose-type glycans at specific regions of high glycan density on MERS-CoV S. Molecular evolution analysis of SARS and MERS S genes also reveals a higher incidence of amino-acid diversity on the exposed surfaces of the S proteins that are not occluded by N-linked glycans. In addition, we compare the structures of the respective glycan coats of SARS and HIV-1 envelope proteins using cryo-electron microscopy (cryo-EM) and computational modelling, which delineate a sparse glycan shield exhibited on SARS S compared with other viral glycoproteins. We therefore undertook a comparative analysis of viral glycan shields from characterized class I fusion proteins to highlight how glycosylation density influences oligomannose-type glycan abundance, and the relationship between effective glycan shields and viral evasion ability. Together, these data underscore the importance of glycosylation in viral immune evasion."}

{"project":"LitCovid-sample-sentences","denotations":[{"id":"T24","span":{"begin":0,"end":250},"obj":"Sentence"},{"id":"T25","span":{"begin":251,"end":471},"obj":"Sentence"},{"id":"T26","span":{"begin":472,"end":666},"obj":"Sentence"},{"id":"T27","span":{"begin":667,"end":942},"obj":"Sentence"},{"id":"T28","span":{"begin":943,"end":1222},"obj":"Sentence"},{"id":"T29","span":{"begin":1223,"end":1311},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Here, we provide global and site-specific analyses of N-linked glycosylation on soluble SARS, MERS and HKU1 CoV S glycoproteins and reveal extensive heterogeneity, ranging from oligomannose-type glycans to highly-processed complex-type glycosylation. The structural mapping of glycans of trimeric S proteins revealed that some of these glycans contribute to the formation of a cluster of oligomannose-type glycans at specific regions of high glycan density on MERS-CoV S. Molecular evolution analysis of SARS and MERS S genes also reveals a higher incidence of amino-acid diversity on the exposed surfaces of the S proteins that are not occluded by N-linked glycans. In addition, we compare the structures of the respective glycan coats of SARS and HIV-1 envelope proteins using cryo-electron microscopy (cryo-EM) and computational modelling, which delineate a sparse glycan shield exhibited on SARS S compared with other viral glycoproteins. We therefore undertook a comparative analysis of viral glycan shields from characterized class I fusion proteins to highlight how glycosylation density influences oligomannose-type glycan abundance, and the relationship between effective glycan shields and viral evasion ability. Together, these data underscore the importance of glycosylation in viral immune evasion."}

{"project":"LitCovid-sample-PD-MONDO","denotations":[{"id":"T19","span":{"begin":88,"end":92},"obj":"Disease"},{"id":"T20","span":{"begin":504,"end":508},"obj":"Disease"},{"id":"T21","span":{"begin":740,"end":744},"obj":"Disease"},{"id":"T22","span":{"begin":895,"end":899},"obj":"Disease"}],"attributes":[{"id":"A19","pred":"mondo_id","subj":"T19","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A20","pred":"mondo_id","subj":"T20","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A21","pred":"mondo_id","subj":"T21","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"},{"id":"A22","pred":"mondo_id","subj":"T22","obj":"http://purl.obolibrary.org/obo/MONDO_0005091"}],"text":"Here, we provide global and site-specific analyses of N-linked glycosylation on soluble SARS, MERS and HKU1 CoV S glycoproteins and reveal extensive heterogeneity, ranging from oligomannose-type glycans to highly-processed complex-type glycosylation. The structural mapping of glycans of trimeric S proteins revealed that some of these glycans contribute to the formation of a cluster of oligomannose-type glycans at specific regions of high glycan density on MERS-CoV S. Molecular evolution analysis of SARS and MERS S genes also reveals a higher incidence of amino-acid diversity on the exposed surfaces of the S proteins that are not occluded by N-linked glycans. In addition, we compare the structures of the respective glycan coats of SARS and HIV-1 envelope proteins using cryo-electron microscopy (cryo-EM) and computational modelling, which delineate a sparse glycan shield exhibited on SARS S compared with other viral glycoproteins. We therefore undertook a comparative analysis of viral glycan shields from characterized class I fusion proteins to highlight how glycosylation density influences oligomannose-type glycan abundance, and the relationship between effective glycan shields and viral evasion ability. Together, these data underscore the importance of glycosylation in viral immune evasion."}

{"project":"LitCovid-sample-Pubtator","denotations":[{"id":"188","span":{"begin":88,"end":92},"obj":"Disease"},{"id":"189","span":{"begin":94,"end":98},"obj":"Disease"},{"id":"171","span":{"begin":108,"end":111},"obj":"Species"},{"id":"174","span":{"begin":177,"end":189},"obj":"Chemical"},{"id":"175","span":{"begin":195,"end":202},"obj":"Chemical"},{"id":"176","span":{"begin":277,"end":284},"obj":"Chemical"},{"id":"177","span":{"begin":336,"end":343},"obj":"Chemical"},{"id":"178","span":{"begin":388,"end":400},"obj":"Chemical"},{"id":"179","span":{"begin":406,"end":413},"obj":"Chemical"},{"id":"180","span":{"begin":442,"end":448},"obj":"Chemical"},{"id":"172","span":{"begin":460,"end":468},"obj":"Species"},{"id":"190","span":{"begin":504,"end":508},"obj":"Disease"},{"id":"191","span":{"begin":513,"end":517},"obj":"Disease"},{"id":"181","span":{"begin":649,"end":665},"obj":"Chemical"},{"id":"182","span":{"begin":724,"end":730},"obj":"Chemical"},{"id":"192","span":{"begin":740,"end":744},"obj":"Disease"},{"id":"173","span":{"begin":749,"end":754},"obj":"Species"},{"id":"183","span":{"begin":868,"end":874},"obj":"Chemical"},{"id":"193","span":{"begin":895,"end":899},"obj":"Disease"},{"id":"184","span":{"begin":998,"end":1004},"obj":"Chemical"},{"id":"185","span":{"begin":1106,"end":1118},"obj":"Chemical"},{"id":"186","span":{"begin":1124,"end":1130},"obj":"Chemical"},{"id":"187","span":{"begin":1181,"end":1187},"obj":"Chemical"}],"attributes":[{"id":"A179","pred":"pubann:denotes","subj":"179","obj":"MESH:D011134"},{"id":"A183","pred":"pubann:denotes","subj":"183","obj":"MESH:D011134"},{"id":"A188","pred":"pubann:denotes","subj":"188","obj":"MESH:D045169"},{"id":"A192","pred":"pubann:denotes","subj":"192","obj":"MESH:D045169"},{"id":"A190","pred":"pubann:denotes","subj":"190","obj":"MESH:D045169"},{"id":"A182","pred":"pubann:denotes","subj":"182","obj":"MESH:D011134"},{"id":"A187","pred":"pubann:denotes","subj":"187","obj":"MESH:D011134"},{"id":"A176","pred":"pubann:denotes","subj":"176","obj":"MESH:D011134"},{"id":"A173","pred":"pubann:denotes","subj":"173","obj":"Tax:11676"},{"id":"A180","pred":"pubann:denotes","subj":"180","obj":"MESH:D011134"},{"id":"A175","pred":"pubann:denotes","subj":"175","obj":"MESH:D011134"},{"id":"A172","pred":"pubann:denotes","subj":"172","obj":"Tax:1335626"},{"id":"A184","pred":"pubann:denotes","subj":"184","obj":"MESH:D011134"},{"id":"A191","pred":"pubann:denotes","subj":"191","obj":"MESH:D018352"},{"id":"A171","pred":"pubann:denotes","subj":"171","obj":"Tax:11118"},{"id":"A193","pred":"pubann:denotes","subj":"193","obj":"MESH:D045169"},{"id":"A189","pred":"pubann:denotes","subj":"189","obj":"MESH:D018352"},{"id":"A177","pred":"pubann:denotes","subj":"177","obj":"MESH:D011134"},{"id":"A186","pred":"pubann:denotes","subj":"186","obj":"MESH:D011134"}],"text":"Here, we provide global and site-specific analyses of N-linked glycosylation on soluble SARS, MERS and HKU1 CoV S glycoproteins and reveal extensive heterogeneity, ranging from oligomannose-type glycans to highly-processed complex-type glycosylation. The structural mapping of glycans of trimeric S proteins revealed that some of these glycans contribute to the formation of a cluster of oligomannose-type glycans at specific regions of high glycan density on MERS-CoV S. Molecular evolution analysis of SARS and MERS S genes also reveals a higher incidence of amino-acid diversity on the exposed surfaces of the S proteins that are not occluded by N-linked glycans. In addition, we compare the structures of the respective glycan coats of SARS and HIV-1 envelope proteins using cryo-electron microscopy (cryo-EM) and computational modelling, which delineate a sparse glycan shield exhibited on SARS S compared with other viral glycoproteins. We therefore undertook a comparative analysis of viral glycan shields from characterized class I fusion proteins to highlight how glycosylation density influences oligomannose-type glycan abundance, and the relationship between effective glycan shields and viral evasion ability. Together, these data underscore the importance of glycosylation in viral immune evasion."}

{"project":"LitCovid-sample-UniProt","denotations":[{"id":"T1718","span":{"begin":112,"end":127},"obj":"Protein"},{"id":"T1817","span":{"begin":297,"end":307},"obj":"Protein"},{"id":"T1850","span":{"begin":613,"end":623},"obj":"Protein"},{"id":"T1883","span":{"begin":755,"end":772},"obj":"Protein"},{"id":"T1887","span":{"begin":928,"end":941},"obj":"Protein"}],"attributes":[{"id":"A1718","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q9QAS2"},{"id":"A1719","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q9QAR5"},{"id":"A1720","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q9QAQ8"},{"id":"A1721","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q9IW04"},{"id":"A1722","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q9IKD1"},{"id":"A1723","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q990M4"},{"id":"A1724","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q990M3"},{"id":"A1725","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q990M2"},{"id":"A1726","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q990M1"},{"id":"A1727","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q91AV1"},{"id":"A1728","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q91A26"},{"id":"A1729","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q8V436"},{"id":"A1730","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q8JSP8"},{"id":"A1731","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q8BB25"},{"id":"A1732","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q86623"},{"id":"A1733","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q85088"},{"id":"A1734","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q85087"},{"id":"A1735","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q80BV6"},{"id":"A1736","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q7TFB1"},{"id":"A1737","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q7TFA2"},{"id":"A1738","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q7TA19"},{"id":"A1739","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q7T6T3"},{"id":"A1740","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q7T696"},{"id":"A1741","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q77NC4"},{"id":"A1742","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q6TNF9"},{"id":"A1743","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q6R1L7"},{"id":"A1744","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q6QU82"},{"id":"A1745","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q6Q1S2"},{"id":"A1746","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q696Q6"},{"id":"A1747","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q66291"},{"id":"A1748","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q66290"},{"id":"A1749","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q66199"},{"id":"A1750","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q66177"},{"id":"A1751","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q66176"},{"id":"A1752","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q66174"},{"id":"A1753","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q65984"},{"id":"A1754","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q5MQD0"},{"id":"A1755","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q5I5X9"},{"id":"A1756","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q5DIY0"},{"id":"A1757","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q5DIX9"},{"id":"A1758","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q5DIX8"},{"id":"A1759","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q5DIX7"},{"id":"A1760","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q52PA3"},{"id":"A1761","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q4ZJS1"},{"id":"A1762","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q4U5G0"},{"id":"A1763","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q3T8J0"},{"id":"A1764","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q3LZX1"},{"id":"A1765","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q3I5J5"},{"id":"A1766","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q14EB0"},{"id":"A1767","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q0ZME7"},{"id":"A1768","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q0Q4F2"},{"id":"A1769","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q0Q475"},{"id":"A1770","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q0Q466"},{"id":"A1771","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q0GNB8"},{"id":"A1772","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q02385"},{"id":"A1773","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q02167"},{"id":"A1774","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q01977"},{"id":"A1775","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/Q008X4"},{"id":"A1776","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P89344"},{"id":"A1777","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P89343"},{"id":"A1778","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P89342"},{"id":"A1779","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P59594"},{"id":"A1780","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P36334"},{"id":"A1781","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P36300"},{"id":"A1782","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P33470"},{"id":"A1783","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P30208"},{"id":"A1784","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P30207"},{"id":"A1785","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P30206"},{"id":"A1786","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P30019"},{"id":"A1787","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P27655"},{"id":"A1788","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P25194"},{"id":"A1789","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P25193"},{"id":"A1790","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P25192"},{"id":"A1791","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P25191"},{"id":"A1792","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P25190"},{"id":"A1793","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P24413"},{"id":"A1794","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P23052"},{"id":"A1795","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P22432"},{"id":"A1796","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P18450"},{"id":"A1797","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P17662"},{"id":"A1798","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P15777"},{"id":"A1799","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P15423"},{"id":"A1800","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P12722"},{"id":"A1801","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P12651"},{"id":"A1802","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P12650"},{"id":"A1803","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P11225"},{"id":"A1804","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P11224"},{"id":"A1805","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P11223"},{"id":"A1806","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P10033"},{"id":"A1807","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P0DTC2"},{"id":"A1808","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P07946"},{"id":"A1809","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P05135"},{"id":"A1810","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/P05134"},{"id":"A1811","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/O90304"},{"id":"A1812","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/O39227"},{"id":"A1813","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/K9N5Q8"},{"id":"A1814","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/A3EXG6"},{"id":"A1815","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/A3EXD0"},{"id":"A1816","pred":"uniprot_id","subj":"T1718","obj":"https://www.uniprot.org/uniprot/A3EX94"},{"id":"A1817","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q9UIP0"},{"id":"A1818","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q9UIN9"},{"id":"A1819","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q9UIN8"},{"id":"A1820","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q9UIN7"},{"id":"A1821","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q9UIN6"},{"id":"A1822","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q9UBH8"},{"id":"A1823","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q9NRH8"},{"id":"A1824","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q9NRH7"},{"id":"A1825","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q9NRH6"},{"id":"A1826","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q9NRH5"},{"id":"A1827","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q9NRH4"},{"id":"A1828","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q9NPG5"},{"id":"A1829","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q9NPE0"},{"id":"A1830","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q9NP52"},{"id":"A1831","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q95IF9"},{"id":"A1832","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q8N5P3"},{"id":"A1833","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q8IZU6"},{"id":"A1834","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q8IZU5"},{"id":"A1835","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q8IZU4"},{"id":"A1836","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q86Z04"},{"id":"A1837","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q7YR44"},{"id":"A1838","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q7LA71"},{"id":"A1839","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q7LA70"},{"id":"A1840","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q5STD2"},{"id":"A1841","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q5SQ85"},{"id":"A1842","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q1XI16"},{"id":"A1843","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q1XI12"},{"id":"A1844","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/Q15517"},{"id":"A1845","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/O43509"},{"id":"A1846","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/O19084"},{"id":"A1847","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/B0UYZ7"},{"id":"A1848","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/B0S7V2"},{"id":"A1849","pred":"uniprot_id","subj":"T1817","obj":"https://www.uniprot.org/uniprot/A5A6L9"},{"id":"A1850","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q9UIP0"},{"id":"A1851","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q9UIN9"},{"id":"A1852","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q9UIN8"},{"id":"A1853","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q9UIN7"},{"id":"A1854","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q9UIN6"},{"id":"A1855","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q9UBH8"},{"id":"A1856","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q9NRH8"},{"id":"A1857","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q9NRH7"},{"id":"A1858","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q9NRH6"},{"id":"A1859","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q9NRH5"},{"id":"A1860","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q9NRH4"},{"id":"A1861","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q9NPG5"},{"id":"A1862","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q9NPE0"},{"id":"A1863","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q9NP52"},{"id":"A1864","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q95IF9"},{"id":"A1865","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q8N5P3"},{"id":"A1866","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q8IZU6"},{"id":"A1867","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q8IZU5"},{"id":"A1868","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q8IZU4"},{"id":"A1869","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q86Z04"},{"id":"A1870","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q7YR44"},{"id":"A1871","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q7LA71"},{"id":"A1872","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q7LA70"},{"id":"A1873","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q5STD2"},{"id":"A1874","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q5SQ85"},{"id":"A1875","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q1XI16"},{"id":"A1876","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q1XI12"},{"id":"A1877","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/Q15517"},{"id":"A1878","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/O43509"},{"id":"A1879","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/O19084"},{"id":"A1880","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/B0UYZ7"},{"id":"A1881","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/B0S7V2"},{"id":"A1882","pred":"uniprot_id","subj":"T1850","obj":"https://www.uniprot.org/uniprot/A5A6L9"},{"id":"A1883","pred":"uniprot_id","subj":"T1883","obj":"https://www.uniprot.org/uniprot/P24123"},{"id":"A1884","pred":"uniprot_id","subj":"T1883","obj":"https://www.uniprot.org/uniprot/P0C782"},{"id":"A1885","pred":"uniprot_id","subj":"T1883","obj":"https://www.uniprot.org/uniprot/P0C781"},{"id":"A1886","pred":"uniprot_id","subj":"T1883","obj":"https://www.uniprot.org/uniprot/C1JJY3"},{"id":"A1887","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q9QSP1"},{"id":"A1888","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q9QJT6"},{"id":"A1889","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q9JGT4"},{"id":"A1890","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q9IPJ6"},{"id":"A1891","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q9DIC6"},{"id":"A1892","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q91DS0"},{"id":"A1893","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q91C28"},{"id":"A1894","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q8QQA2"},{"id":"A1895","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q8QPE5"},{"id":"A1896","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q8QPE4"},{"id":"A1897","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q8QPE3"},{"id":"A1898","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q8JTH0"},{"id":"A1899","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q8BDV6"},{"id":"A1900","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q8B6J6"},{"id":"A1901","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q8B0I1"},{"id":"A1902","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q8B0H6"},{"id":"A1903","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q8B0H1"},{"id":"A1904","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q89669"},{"id":"A1905","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q85213"},{"id":"A1906","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q82706"},{"id":"A1907","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q82683"},{"id":"A1908","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q82020"},{"id":"A1909","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q787B5"},{"id":"A1910","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q77SK0"},{"id":"A1911","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q77N36"},{"id":"A1912","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q76G52"},{"id":"A1913","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q75T09"},{"id":"A1914","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q6X1D5"},{"id":"A1915","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q6X1D1"},{"id":"A1916","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q6TYA0"},{"id":"A1917","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q6E0W7"},{"id":"A1918","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q66T62"},{"id":"A1919","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q5VKP3"},{"id":"A1920","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q5VKN9"},{"id":"A1921","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q5K2K4"},{"id":"A1922","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q5IX93"},{"id":"A1923","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q5IX92"},{"id":"A1924","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q5IX91"},{"id":"A1925","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q5IX90"},{"id":"A1926","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q5IX89"},{"id":"A1927","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q5IX88"},{"id":"A1928","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q5IX87"},{"id":"A1929","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q5GA86"},{"id":"A1930","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q58FH1"},{"id":"A1931","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q4VKV3"},{"id":"A1932","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q4F900"},{"id":"A1933","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q49LL3"},{"id":"A1934","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q49IU2"},{"id":"A1935","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q49IU1"},{"id":"A1936","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q49IT9"},{"id":"A1937","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q49IT8"},{"id":"A1938","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q49AV0"},{"id":"A1939","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q0GBY1"},{"id":"A1940","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q0GBX6"},{"id":"A1941","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/Q08089"},{"id":"A1942","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/P32595"},{"id":"A1943","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/P32550"},{"id":"A1944","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/P19462"},{"id":"A1945","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/P16288"},{"id":"A1946","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/P15199"},{"id":"A1947","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/P13180"},{"id":"A1948","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/P0C572"},{"id":"A1949","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/P08667"},{"id":"A1950","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/P08163"},{"id":"A1951","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/P07923"},{"id":"A1952","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/P04884"},{"id":"A1953","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/P04883"},{"id":"A1954","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/P04882"},{"id":"A1955","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/P03524"},{"id":"A1956","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/P03522"},{"id":"A1957","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/O92284"},{"id":"A1958","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/O56677"},{"id":"A1959","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/O10236"},{"id":"A1960","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/J7HBH4"},{"id":"A1961","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/D8V075"},{"id":"A1962","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/A7WNB3"},{"id":"A1963","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/A4UHQ6"},{"id":"A1964","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/A4UHQ1"},{"id":"A1965","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/A3RM22"},{"id":"A1966","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/A3F5R8"},{"id":"A1967","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/A3F5R3"},{"id":"A1968","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/A3F5Q8"},{"id":"A1969","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/A3F5N3"},{"id":"A1970","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/A3F5M3"},{"id":"A1971","pred":"uniprot_id","subj":"T1887","obj":"https://www.uniprot.org/uniprot/A3F5L8"}],"text":"Here, we provide global and site-specific analyses of N-linked glycosylation on soluble SARS, MERS and HKU1 CoV S glycoproteins and reveal extensive heterogeneity, ranging from oligomannose-type glycans to highly-processed complex-type glycosylation. The structural mapping of glycans of trimeric S proteins revealed that some of these glycans contribute to the formation of a cluster of oligomannose-type glycans at specific regions of high glycan density on MERS-CoV S. Molecular evolution analysis of SARS and MERS S genes also reveals a higher incidence of amino-acid diversity on the exposed surfaces of the S proteins that are not occluded by N-linked glycans. In addition, we compare the structures of the respective glycan coats of SARS and HIV-1 envelope proteins using cryo-electron microscopy (cryo-EM) and computational modelling, which delineate a sparse glycan shield exhibited on SARS S compared with other viral glycoproteins. We therefore undertook a comparative analysis of viral glycan shields from characterized class I fusion proteins to highlight how glycosylation density influences oligomannose-type glycan abundance, and the relationship between effective glycan shields and viral evasion ability. Together, these data underscore the importance of glycosylation in viral immune evasion."}

{"project":"LitCovid-sample-PD-GO-BP-0","denotations":[{"id":"T14","span":{"begin":63,"end":76},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T15","span":{"begin":236,"end":249},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T16","span":{"begin":362,"end":371},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T17","span":{"begin":1073,"end":1086},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T18","span":{"begin":1273,"end":1286},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T19","span":{"begin":1296,"end":1310},"obj":"http://purl.obolibrary.org/obo/GO_0020012"},{"id":"T20","span":{"begin":1296,"end":1310},"obj":"http://purl.obolibrary.org/obo/GO_0051805"}],"text":"Here, we provide global and site-specific analyses of N-linked glycosylation on soluble SARS, MERS and HKU1 CoV S glycoproteins and reveal extensive heterogeneity, ranging from oligomannose-type glycans to highly-processed complex-type glycosylation. The structural mapping of glycans of trimeric S proteins revealed that some of these glycans contribute to the formation of a cluster of oligomannose-type glycans at specific regions of high glycan density on MERS-CoV S. Molecular evolution analysis of SARS and MERS S genes also reveals a higher incidence of amino-acid diversity on the exposed surfaces of the S proteins that are not occluded by N-linked glycans. In addition, we compare the structures of the respective glycan coats of SARS and HIV-1 envelope proteins using cryo-electron microscopy (cryo-EM) and computational modelling, which delineate a sparse glycan shield exhibited on SARS S compared with other viral glycoproteins. We therefore undertook a comparative analysis of viral glycan shields from characterized class I fusion proteins to highlight how glycosylation density influences oligomannose-type glycan abundance, and the relationship between effective glycan shields and viral evasion ability. Together, these data underscore the importance of glycosylation in viral immune evasion."}

{"project":"LitCovid-sample-GO-BP","denotations":[{"id":"T12","span":{"begin":63,"end":76},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T13","span":{"begin":236,"end":249},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T14","span":{"begin":362,"end":371},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T15","span":{"begin":1073,"end":1086},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T16","span":{"begin":1273,"end":1286},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T17","span":{"begin":1296,"end":1310},"obj":"http://purl.obolibrary.org/obo/GO_0042783"}],"text":"Here, we provide global and site-specific analyses of N-linked glycosylation on soluble SARS, MERS and HKU1 CoV S glycoproteins and reveal extensive heterogeneity, ranging from oligomannose-type glycans to highly-processed complex-type glycosylation. The structural mapping of glycans of trimeric S proteins revealed that some of these glycans contribute to the formation of a cluster of oligomannose-type glycans at specific regions of high glycan density on MERS-CoV S. Molecular evolution analysis of SARS and MERS S genes also reveals a higher incidence of amino-acid diversity on the exposed surfaces of the S proteins that are not occluded by N-linked glycans. In addition, we compare the structures of the respective glycan coats of SARS and HIV-1 envelope proteins using cryo-electron microscopy (cryo-EM) and computational modelling, which delineate a sparse glycan shield exhibited on SARS S compared with other viral glycoproteins. We therefore undertook a comparative analysis of viral glycan shields from characterized class I fusion proteins to highlight how glycosylation density influences oligomannose-type glycan abundance, and the relationship between effective glycan shields and viral evasion ability. Together, these data underscore the importance of glycosylation in viral immune evasion."}

{"project":"LitCovid-PD-GO-BP","denotations":[{"id":"T13","span":{"begin":54,"end":76},"obj":"http://purl.obolibrary.org/obo/GO_0006487"},{"id":"T14","span":{"begin":63,"end":76},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T15","span":{"begin":236,"end":249},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T16","span":{"begin":362,"end":371},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T17","span":{"begin":1073,"end":1086},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T18","span":{"begin":1273,"end":1286},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T19","span":{"begin":1296,"end":1310},"obj":"http://purl.obolibrary.org/obo/GO_0042783"}],"text":"Here, we provide global and site-specific analyses of N-linked glycosylation on soluble SARS, MERS and HKU1 CoV S glycoproteins and reveal extensive heterogeneity, ranging from oligomannose-type glycans to highly-processed complex-type glycosylation. The structural mapping of glycans of trimeric S proteins revealed that some of these glycans contribute to the formation of a cluster of oligomannose-type glycans at specific regions of high glycan density on MERS-CoV S. Molecular evolution analysis of SARS and MERS S genes also reveals a higher incidence of amino-acid diversity on the exposed surfaces of the S proteins that are not occluded by N-linked glycans. In addition, we compare the structures of the respective glycan coats of SARS and HIV-1 envelope proteins using cryo-electron microscopy (cryo-EM) and computational modelling, which delineate a sparse glycan shield exhibited on SARS S compared with other viral glycoproteins. We therefore undertook a comparative analysis of viral glycan shields from characterized class I fusion proteins to highlight how glycosylation density influences oligomannose-type glycan abundance, and the relationship between effective glycan shields and viral evasion ability. Together, these data underscore the importance of glycosylation in viral immune evasion."}

{"project":"LitCovid-sentences","denotations":[{"id":"T24","span":{"begin":0,"end":250},"obj":"Sentence"},{"id":"T25","span":{"begin":251,"end":471},"obj":"Sentence"},{"id":"T26","span":{"begin":472,"end":666},"obj":"Sentence"},{"id":"T27","span":{"begin":667,"end":942},"obj":"Sentence"},{"id":"T28","span":{"begin":943,"end":1222},"obj":"Sentence"},{"id":"T29","span":{"begin":1223,"end":1311},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Here, we provide global and site-specific analyses of N-linked glycosylation on soluble SARS, MERS and HKU1 CoV S glycoproteins and reveal extensive heterogeneity, ranging from oligomannose-type glycans to highly-processed complex-type glycosylation. The structural mapping of glycans of trimeric S proteins revealed that some of these glycans contribute to the formation of a cluster of oligomannose-type glycans at specific regions of high glycan density on MERS-CoV S. Molecular evolution analysis of SARS and MERS S genes also reveals a higher incidence of amino-acid diversity on the exposed surfaces of the S proteins that are not occluded by N-linked glycans. In addition, we compare the structures of the respective glycan coats of SARS and HIV-1 envelope proteins using cryo-electron microscopy (cryo-EM) and computational modelling, which delineate a sparse glycan shield exhibited on SARS S compared with other viral glycoproteins. We therefore undertook a comparative analysis of viral glycan shields from characterized class I fusion proteins to highlight how glycosylation density influences oligomannose-type glycan abundance, and the relationship between effective glycan shields and viral evasion ability. Together, these data underscore the importance of glycosylation in viral immune evasion."}